Results 121 to 130 of about 16,120 (166)
Effect of chokeberry pomace as a feed additive for high-producing dairy goats on oxidative stress parameters and quality of milk. [PDF]
J Vet ResSzymańska-Czerwińska M +9 more
europepmc +1 more source
Integrative In Silico and In Vitro Evaluation of Vialox and Leuphasyl Pentapeptides for Antiaging Applications. [PDF]
Chem BiodiversAkhan D +4 more
europepmc +1 more source
The Journal of biological chemistry, 1996 E K, PATTERSON, S H, HSIAO, A, KEPPEL
openaire +1 more source
[SERUM LEUCYL-AMINOPEPTIDASE ACTIVITY IN DISEASES OF THE LIVER, BILE DUCTS AND PANCREAS].
Przeglad epidemiologiczny, 1996 openaire +1 more source
Characterisation of Leucyl Aminopeptidase From Solanum tuberosum Tuber
Food Chemistry, 2010 Abstract Potato juice (a waste product from the starch industry) is a potential source of novel enzymes for food applications. For use in the production and improvement of food protein hydrolysates, commercially available exopeptidases, predominantly aminopeptidases, are recommended.
Miroslava Vujčić +2 more
exaly +5 more sources
Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology, 2003 Exopeptidases of Morimus funereus larvae were partially purified and characterized. Specific leucyl aminopeptidase (LAP) activity was increased eight-fold by gel filtration of the crude midgut extract. The partially purified LAP had a molecular mass greater than 100 kDa with pH optima from 7.0-9.0 and no strict substrate specificity. M.
Nataša Božić +2 more
exaly +6 more sources
Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology, 2008 The major leucyl aminopeptidase (LAP) from the midgut of Morimus funereus larvae was purified and characterised. Specific LAP activity was increased 292-fold by purification of the crude midgut extract. The purified enzyme had a pH optimum of 7.5 (optimum pH range 7.0-8.5) and preferentially hydrolysed p-nitroanilides containing hydrophobic amino acids
Nataša Božić +2 more
exaly +9 more sources
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Clinica Chimica Acta, 1991
The purification and characterization of leucyl aminopeptidase and pyroglutamyl aminopeptidase from human skeletal muscle are described. The characteristics of leucyl aminopeptidase were as follows: optimum activity was at pH 9.5 in the presence of 5 mmol/l Mg2+ or 0.5 mmol Mn2+. No activation of enzyme activity was obtained following addition of other
Brenda Lauffart, David Mantle, D Mantle
exaly +3 more sources
The purification and characterization of leucyl aminopeptidase and pyroglutamyl aminopeptidase from human skeletal muscle are described. The characteristics of leucyl aminopeptidase were as follows: optimum activity was at pH 9.5 in the presence of 5 mmol/l Mg2+ or 0.5 mmol Mn2+. No activation of enzyme activity was obtained following addition of other
Brenda Lauffart, David Mantle, D Mantle
exaly +3 more sources
Biochemical and Biophysical Research Communications, 1991
Prolyl aminopeptidase (EC 3.4.11.5) has been assumed to be a unique enzyme catalyzing specifically the removal of unsubstituted NH2-terminal L-prolyl residues from various peptides and to be distinct from leucyl aminopeptidase (EC 3.4.11.1). In the present study, prolyl aminopeptidases were purified to apparent homogeneity from pig small intestine ...
M, Matsushima +5 more
openaire +2 more sources
Prolyl aminopeptidase (EC 3.4.11.5) has been assumed to be a unique enzyme catalyzing specifically the removal of unsubstituted NH2-terminal L-prolyl residues from various peptides and to be distinct from leucyl aminopeptidase (EC 3.4.11.1). In the present study, prolyl aminopeptidases were purified to apparent homogeneity from pig small intestine ...
M, Matsushima +5 more
openaire +2 more sources